ID A0A556QJU8_9BACT Unreviewed; 860 AA.
AC A0A556QJU8;
DT 16-OCT-2019, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2019, sequence version 1.
DT 13-SEP-2023, entry version 16.
DE RecName: Full=Chaperone protein ClpB {ECO:0000256|RuleBase:RU362034};
GN Name=clpB {ECO:0000256|RuleBase:RU362034,
GN ECO:0000313|EMBL:TSJ76924.1};
GN ORFNames=FPL22_12465 {ECO:0000313|EMBL:TSJ76924.1};
OS Rariglobus hedericola.
OC Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Rariglobus.
OX NCBI_TaxID=2597822 {ECO:0000313|EMBL:TSJ76924.1, ECO:0000313|Proteomes:UP000315648};
RN [1] {ECO:0000313|EMBL:TSJ76924.1, ECO:0000313|Proteomes:UP000315648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=53C-WASEF {ECO:0000313|EMBL:TSJ76924.1,
RC ECO:0000313|Proteomes:UP000315648};
RA Pitt A., Hahn M.W.;
RT "Description of 53C-WASEF.";
RL Submitted (JUL-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Part of a stress-induced multi-chaperone system, it is
CC involved in the recovery of the cell from heat-induced damage, in
CC cooperation with DnaK, DnaJ and GrpE. {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBUNIT: Homohexamer. The oligomerization is ATP-dependent.
CC {ECO:0000256|ARBA:ARBA00026057}.
CC -!- SUBUNIT: Homohexamer; The oligomerization is ATP-dependent.
CC {ECO:0000256|RuleBase:RU362034}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU362034}.
CC -!- SIMILARITY: Belongs to the ClpA/ClpB family.
CC {ECO:0000256|ARBA:ARBA00008675, ECO:0000256|RuleBase:RU004432}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:TSJ76924.1}.
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DR EMBL; VMBG01000002; TSJ76924.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A556QJU8; -.
DR OrthoDB; 9803641at2; -.
DR Proteomes; UP000315648; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0042026; P:protein refolding; IEA:UniProtKB-UniRule.
DR GO; GO:0009408; P:response to heat; IEA:UniProtKB-UniRule.
DR CDD; cd00009; AAA; 1.
DR CDD; cd19499; RecA-like_ClpB_Hsp104-like; 1.
DR Gene3D; 1.10.8.60; -; 1.
DR Gene3D; 1.10.1780.10; Clp, N-terminal domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR003959; ATPase_AAA_core.
DR InterPro; IPR017730; Chaperonin_ClpB.
DR InterPro; IPR019489; Clp_ATPase_C.
DR InterPro; IPR036628; Clp_N_dom_sf.
DR InterPro; IPR004176; Clp_R_dom.
DR InterPro; IPR001270; ClpA/B.
DR InterPro; IPR018368; ClpA/B_CS1.
DR InterPro; IPR028299; ClpA/B_CS2.
DR InterPro; IPR041546; ClpA/ClpB_AAA_lid.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR03346; chaperone_ClpB; 1.
DR PANTHER; PTHR11638; ATP-DEPENDENT CLP PROTEASE; 1.
DR PANTHER; PTHR11638:SF18; HEAT SHOCK PROTEIN 104; 1.
DR Pfam; PF00004; AAA; 1.
DR Pfam; PF07724; AAA_2; 1.
DR Pfam; PF17871; AAA_lid_9; 1.
DR Pfam; PF02861; Clp_N; 2.
DR Pfam; PF10431; ClpB_D2-small; 1.
DR PRINTS; PR00300; CLPPROTEASEA.
DR SMART; SM00382; AAA; 2.
DR SMART; SM01086; ClpB_D2-small; 1.
DR SUPFAM; SSF81923; Double Clp-N motif; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51903; CLP_R; 1.
DR PROSITE; PS00870; CLPAB_1; 1.
DR PROSITE; PS00871; CLPAB_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004432};
KW Chaperone {ECO:0000256|ARBA:ARBA00023186, ECO:0000256|RuleBase:RU004432};
KW Coiled coil {ECO:0000256|ARBA:ARBA00023054, ECO:0000256|RuleBase:RU362034};
KW Cytoplasm {ECO:0000256|RuleBase:RU362034};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004432};
KW Reference proteome {ECO:0000313|Proteomes:UP000315648};
KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|PROSITE-
KW ProRule:PRU01251}; Stress response {ECO:0000256|RuleBase:RU362034}.
FT DOMAIN 3..150
FT /note="Clp R"
FT /evidence="ECO:0000259|PROSITE:PS51903"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 409..503
FT /evidence="ECO:0000256|RuleBase:RU362034"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 860 AA; 95849 MW; 1C6FD325B0F5A360 CRC64;
MDSNQLTQMS RQAVTDAQAE ARRRSHNEVE TWHLLHALLA QENGIVPALV EKLGLTTSAL
QLAAERELDR LPKVSGSVDT SKVYVTQSVN EVLTRAEAEA KSLKDDFVSV EHLFLGLLDV
AKPDALKNYF KSFGIERTKV LKSLKDLRGA QRVTTDNPET TYAALTKYGI DLVELAKKGK
MDPVIGRDDE IRRTVRILSR KTKNNPVLIG EPGVGKTAIV EGLAQRIVRG DVPEGLKDKT
IFSLDMGALV AGAKYRGEFE ERLKAVLNEV KQADGRIILF IDELHTIVGA GKSDGAMDAG
NLLKPMLARG ELHCIGATTL DEYRQHIEKD AALERRFQPV MVEPPSVEDA ISILRGIRER
FELHHGVRIQ DNALVAAVTL SNRYISDRFL PDKAIDLMDE ACAMIRTEMD SAPQELDALQ
RRVLQLEIEE AALKLEKDDA SKHRLESLRK ELADARSQAA GLKAKWDKEK DSVNAVRAVR
EQLDAARIEL EKAERNYDLN KLAELRHGKI PQLEAELKKS ETTAAKTELF KEEVSAEEIA
EIVSKWSGVP VTRFVEGEKE KLLRLGEVLH ERVIGQDEAV TLATDAILRA RAGIKDPRRP
VGSFLFLGPT GVGKTELAKT LAETLFDSEA ALVRIDMSEY MEKHSVSRLV GAPPGYIGYD
EGGQLTEAVR RKPYAVILFD EIEKAHPDVF NILLQVLDDG RITDSQGRTI DFKNTVIILT
SNLGSRYLIE GVTTDVIPES VRESVMAEVR KAFRPEFLNR IDETILFKPL TLEEITRIVD
LLLADLNKRL LDRRVTVMLD KTAKAWVGEK GYDPVYGARP LKRFLQRQIE TKLARALIGG
EVKDGAEVTF KVQGDELVIA
//